ID IF2_SYNWW Reviewed; 882 AA.
AC Q0AYI8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Swol_0900;
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen;
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; CP000448; ABI68216.1; -; Genomic_DNA.
DR RefSeq; WP_011640321.1; NC_008346.1.
DR AlphaFoldDB; Q0AYI8; -.
DR SMR; Q0AYI8; -.
DR STRING; 335541.Swol_0900; -.
DR KEGG; swo:Swol_0900; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_2_9; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000001968; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..882
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008366"
FT DOMAIN 383..556
FT /note="tr-type G"
FT REGION 38..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..399
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 417..421
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 438..441
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 492..495
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 528..530
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 45..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 392..399
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 438..442
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 492..495
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 882 AA; 97143 MW; 1C6F1C469A0FA607 CRC64;
MAKIRVHELA KELGIASKEM VEVLVELGLD VKNHMSTIED SQASWVKKRL SKSDEDSKKQ
PAQPVTRDEA VKKHSGEPAT QTTQKKPDNP RHVSGPRPQE GSKPSGSTGR REFSENREQS
RKGEERHSAN PRPGTQMKSP RNNAPRPTTR PENRSAGATG RTDNRAPGAA GRTDNRAPGA
VGRTDNRGAG SASRPDNRVT RPAAGRPDNK GSRPSDAKRP PQRTVPGNTP RPVSSPERTT
EKKPGEASRT LPGGAKTAGD KKAFRKNTPA FGQYQSKDYS RPGRKSKHKR KKENIEFQTP
ENIKIEGSIM VRDLAEKLNK NPAEIMKKLM ELGIMATINQ NIDFETAEIV SSLYDVKVER
ELSEEEKILE ELVDIDDDAE LIARPPVVTI MGHVDHGKTS LLDRIRQANV VSGEAGGITQ
HIGAYQVTIK NNKITFIDTP GHEAFTAMRA RGANLTDIVI LVVAADDGVM PQTVEAINHI
RAAKVPFLVA INKIDKPQAD PERIKQQLTE YNIVPEEWGG DTIFVPVSAK SGEGIENLLE
MILLVAEMNE IRANPDRAAY GLVVEGELDK GRGAVATVLV LNGTLNIGDY IICGTNWCRV
RAMIDDRGKR VDKALPSMPV EIMGWSGVPE AGGKVQVCDE KVAKEIIGLR LSEKKIEEQK
QSSRVSLDEF FQQMKDAEVK ELTLIIKGDV QGSVEALRQS LLRLATNEVK VNVIHSAVGA
ITETDVMLAS ASNAIIIGFN VRPDSKARKY AEDEKIDVRM YRVIYEAIDD VKKAMSGLLD
PEYKEKFLGR AEVRALFKVP HVGVIAGSYV IDGKIQRNAS VRVLRDGVIV YEGQLSSLKR
FKDDAKEVVE NYECGIGIKD FNDVKEGDII EAYTLEEIPR EL
//
